C. Greenwood

发表

Some spectral and steady-state kinetic properties of Pseudomonas cytochrome oxidase.

D. Barber, S. R. Parr, C. Greenwood, 1976, The Biochemical journal.

Fast cytochrome bo from Escherichia coli binds two molecules of nitric oxide at CuB.

A. Thomson, H. Seward, C. Butler, 1997, Biochemistry.

Nucleotide sequence encoding the di‐haem cytochrome c 551 peroxidase from Pseudomonas aeruginosa

R. James, C. Ridout, C. Greenwood, 1995, FEBS letters.

Interactions of sulphide and other ligands with cytochrome c oxidase. An electron-paramagnetic-resonance study.

P. Nicholls, A. Thomson, B. Hill, 1984, The Biochemical journal.

Identification of the ligand-exchange process in the alkaline transition of horse heart cytochrome c.

A. Thomson, P. Gadsby, J. Peterson, 1987, The Biochemical journal.

Redox-linked spin-state changes in the di-haem cytochrome c-551 peroxidase from Pseudomonas aeruginosa.

A. Thomson, P. Gadsby, J. Peterson, 1985, The Biochemical journal.

The nature of species prepared by photolysis of half-reduced, fully reduced and fully reduced carbonmonoxy-cytochrome c-551 peroxidase from Pseudomonas aeruginosa.

A. Thomson, J. Peterson, N. Foote, 1984, Biochemical Journal.

Magnetic Circular Dichroism of Hemoproteins

A. Thomson, M. Cheesman, C. Greenwood, 1991 .

Magnetic Circular Dichroism of Hemoproteins.

A. Thomson, M. Cheesman, C. Greenwood, 1991 .

The nature of haem a3 in the oxidized state of cytochrome c oxidase. Evidence from low-temperature magnetic-circular-dichroism spectroscopy in the near infrared region.

A. Thomson, B. Hill, C. Greenwood, 1982, The Biochemical journal.

Structural heterogeneity of Pseudomonas aeruginosa bacterioferritin.

G. Moore, J. Findlay, A. Thomson, 1994, The Biochemical journal.

Redesign of the interior hydrophilic region of mitochondrial cytochrome c by site-directed mutagenesis.

G. Moore, A. Mauk, M. Smith, 1993, Biochemistry.

A re-evaluation of some basic structural and functional properties of Pseudomonas cytochrome oxidase.

M. Brunori, A. Colosimo, T. A. Walsh, 1979, The Biochemical journal.

An investigation of the ligand-binding properties of Pseudomonas aeruginosa nitrite reductase.

A. Thomson, J. Sutherland, J. Peterson, 1986, The Biochemical journal.

Electron paramagnetic resonance studies on Pseudomonas nitrosyl nitrite reductase. Evidence for multiple species in the electron paramagnetic resonance spectra of nitrosyl haemoproteins.

T. A. Walsh, A. Thomson, D. Barber, 1980, The Biochemical journal.

Some magnetic properties of Pseudomonas cytochrome oxidase.

T. A. Walsh, A. Thomson, D. Barber, 1979, The Biochemical journal.

The electron-transfer reaction between azurin and the cytochrome c oxidase from Pseudomonas aeruginosa.

M. Brunori, D. Barber, S. R. Parr, 1977, The Biochemical journal.

Electron transfer kinetics of caa3 oxidase from Bacillus stearothermophilus: a hypothesis for thermophilicity.

M. Brunori, W. Konings, A. Giuffrè, 1999, Biophysical journal.

Electron transfer between cytochrome c and the isolated CuA domain: identification of substrate-binding residues in cytochrome c oxidase.

M. Saraste, P. Lappalainen, N. Watmough, 1995, Biochemistry.

E.p.r. and magnetic circular dichroism spectroscopic characterization of bacterioferritin from Pseudomonas aeruginosa and Azotobacter vinelandii.

G. Moore, A. Thomson, M. Cheesman, 1992, The Biochemical journal.

Determination of the optical properties of CuA(II) in bovine cytochrome c oxidase using magnetic circular dichroism as an optical detector of paramagnetic resonance.

C. P. Barrett, A. Thomson, J. Peterson, 1986, Journal of inorganic biochemistry.

The optical properties of CuA in bovine cytochrome c oxidase determined by low-temperature magnetic-circular-dichroism spectroscopy.

A. Thomson, D. Barber, B. Hill, 1983, The Biochemical journal.

Studies on partially reduced mammalian cytochrome oxidase reactions with ferrocytochrome c.

T. Brittain, C. Greenwood, 1976, The Biochemical journal.

KINETIC OBSERVATIONS ON THE NEAR INFRARED BAND OF CYTOCHROME C OXIDASE.

C. Greenwood, Q. H. Gibson, 1965, The Journal of biological chemistry.

Reactions of cytochrome oxidase with oxygen and carbon monoxide.

C. Greenwood, Q. H. Gibson, 1963, The Biochemical journal.

Low temperature magnetic circular dichroism spectra and magnetization properties of extracted heme a3+ bis-imidazole. A model of cytochrome a in bovine cytochrome c oxidase.

A. Thomson, B. Hill, C. Greenwood, 1984, Journal of inorganic biochemistry.

Kinetic Studies on Mammalian Cytochrome c Oxidase

M. Brunori, Michael T. Wilson, E. Antonini, 1973 .

Purification and properties of formate dehydrogenase from Pseudomonas aeruginosa. Electron-paramagnetic-resonance studies on the molybdenum centre.

A. Thomson, P. Gadsby, A. Coddington, 1987, The Biochemical journal.

Electron-paramagnetic-resonance spectroscopy studies on the dissimilatory nitrate reductase from Pseudomonas aeruginosa.

G. George, A. Thomson, R. Bray, 1984, The Biochemical journal.

Studies of an acid-induced species of purple membrane from Halobacterium halobium.

R. Perham, M. Edgerton, T. Moore, 1978, The Biochemical journal.

Regulatory properties of reduced nicotinamide-adenine dinucleotide phosphate on a glutamate dehydrogenase from Neurospora crassa

M. Gore, C. Greenwood, 1975 .

Studies on the binary and ternary complexes formed by a Neurospora glutamate dehydrogenase and its substrates.

M. Gore, C. Greenwood, 1975, Biochemical and biophysical research communications.

Variable-temperature magnetic-circular-dichroism spectra of cytochrome c oxidase and its derivatives.

A. Thomson, T. Brittain, C. Greenwood, 1977, The Biochemical journal.

Studies on partially reduced mammalian cytochrome oxidase. Reactions with carbon monoxide and oxygen.

M. Brunori, M. Wilson, C. Greenwood, 1974, The Biochemical journal.

The reaction of fully reduced cytochrome c oxidase with oxygen studied by flow-flash spectrophotometry at room temperature. Evidence for new pathways of electron transfer.

B. Hill, C. Greenwood, 1984, The Biochemical journal.

Spectroscopic evidence for the participation of compound A (Fea32+-O2) in the reaction of mixed-valence cytochrome c oxidase with oxygen at room temperature.

B. Hill, C. Greenwood, 1983, The Biochemical journal.

EVIDENCE FOR HIGH ENERGY STORAGE INTERMEDIATES IN BIOLUMINESCENCE

J. W. Hastings, Q. Gibson, C. Greenwood, 1965 .

The reaction of Pseudomonas aeruginosa cytochrome c-551 oxidase with oxygen.

M. Brunori, A. Colosimo, E. Antonini, 1978, The Biochemical journal.

A purification procedure for the soluble cytochrome oxidase and some other respiratory proteins from Pseudomonas aeruginosa.

D. Barber, S. R. Parr, C. Greenwood, 1976, The Biochemical journal.

A temperature-jump study of the reaction between azurin and cytochrome c oxidase from Pseudomonas aeruginosa.

M. Brunori, M. Wilson, S. R. Parr, 1975, The Biochemical journal.

Evidence for the existence of two functionally distinct forms cytochrome c manomer at alkaline pH.

G. Palmer, C. Greenwood, 1965, The Journal of biological chemistry.

The structure of the cytochrome a3-CuB site of mammalian cytochrome c oxidase as probed by MCD and EPR spectroscopy.

P. Nicholls, A. Thomson, B. Hill, 1985, Journal of inorganic biochemistry.

Studies of the primary oxygen intermediate in the reaction of fully reduced cytochrome oxidase.

Q. Gibson, R. Blackmore, C. Greenwood, 1991, The Journal of biological chemistry.

The nature of ferrous haem protein complexes prepared by photolysis

A. Thomson, T. Brittain, C. Greenwood, 1982 .

Catalytic Mechanism of Cytochrome Oxidase

M. Brunori, E. Antonini, B. Malmström, 1970, Nature.

Cytochrome bo from Escherichia coli: reaction of the oxidized enzyme with hydrogen peroxide.

A. Thomson, M. Cheesman, N. Watmough, 1994, The Biochemical journal.

Distinct forms of the haem o‐Cu binuclear site of oxidised cytochrome bo from Escherichia coli

R. Gennis, A. Thomson, M. Cheesman, 1993, FEBS letters.

A conserved glutamic acid in helix VI of cytochrome bo3 influences a key step in oxygen reduction.

R. Gennis, A. Katsonouri, R. Little, 1997, Biochemistry.

Reaction of variant sperm-whale myoglobins with hydrogen peroxide: the effects of mutating a histidine residue in the haem distal pocket.

A. R. Baker, D. Lowe, R. Little, 1997, The Biochemical journal.

An investigation of the co-operative binding of carbon monoxide to the haemoglobin of the carpet shark Cephaloscyllium.

D. Barber, T. Brittain, R. Wells, 1982, Comparative biochemistry and physiology. B, Comparative biochemistry.

An investigation of the allosteric functioning of the haemoglobin of the cane toad, Bufo marinus.

D. Barber, T. Brittain, R. Wells, 1982, Comparative biochemistry and physiology. B, Comparative biochemistry.

Studies on ferricytochrome c. I. Effect of pH, ionic strength and protein denaturants on the spectra of ferricytochrome c.

M. Wilson, C. Greenwood, 1971, European journal of biochemistry.

The synthesis of 4 - Substituted Indoles via arenetricarbonylchromium(0) complexes

P. Beswick, D. Widdowson, G. Nechvatal, 1988 .

Cytochrome bo from Escherichia coli: identification of haem ligands and reaction of the reduced enzyme with carbon monoxide.

R. Gennis, A. Thomson, C. A. Pires, 1993, The Biochemical journal.

Studies on Ferricytochrome c

Michael T. Wilson, C. Greenwood, 1971 .

Bacterial nitrite-reducing enzymes.

A. Thomson, R. Blackmore, T. Brittain, 1992, European journal of biochemistry.

Optical detection of paramagnetic resonance by magnetic circular dichroism. Applications to aqueous solutions of metalloproteins

C. P. Barrett, A. Thomson, J. Peterson, 1986 .

Intermediate steps in the reaction of cytochrome oxidase with molecular oxygen.

P. Nicholls, B. Hill, C. Greenwood, 1986, Biochimica et biophysica acta.

THE REACTION OF CYTOCHROME OXIDASE WITH CYTOCHROME C.

C. Greenwood, Q. H. Gibson, Q. H. Gibson, 1965, The Journal of biological chemistry.

Electron transfer between azurin and cytochrone c-551 from Pseudomonas aeruginosa.

M. Brunori, M. Wilson, E. Antonini, 1975, The Biochemical journal.

Magnetic-circular-dichroism studies of Escherichia coli cytochrome bo. Identification of high-spin ferric, low-spin ferric and ferryl [Fe(IV)] forms of heme o.

R. Gennis, A. Thomson, M. Cheesman, 1994, European journal of biochemistry.

A study of the magnetic properties of haem a3 in cytochrome c oxidase by using magnetic-circular-dichroism spectroscopy.

A. Thomson, C. Greenwood, P. E. Gooding, 1981, The Biochemical journal.

Change in charge of an unvaried heme contact residue does not cause a major change of conformation in cytochrome c

G. Moore, G. Pielak, A. Davies, 1991, FEBS letters.

The interaction of cyanide with cytochrome oxidase.

M. Brunori, E. Antonini, B. Malmström, 1971, European journal of biochemistry.

Preparation of Thieno[3,2-e][1,2]oxazepine, Thieno and [1]Benzothieno-[3,2-g][1,4]oxazonine, and 5H-Thieno and 1H-[1]Benzothieno-[3,2-h][1,5]oxazecine Derivatives by Ring Expansion Methods. X-Ray Crystal Structure of 1-Phenyl-1,3,4,5,6,7-hexahydro[1]benzothieno-[3,2-g][1,4]oxazonine-5-carbonitrile

A. White, L. M. Engelhardt, J. Bremner, 1988 .

Preparation of Thieno(3,2‐e)(1,2)oxazepine, Thieno‐ and (1)Benzothieno‐(3,2‐g)(1,4)oxazonine, and 5H‐Thieno‐ and 1H‐(1)Benzothieno(3,2‐h)(1,5)oxazecine Derivatives by Ring Expansion Methods. X‐Ray Crystal Structure of 1‐Phenyl‐1,3,4,5,6,7‐hexahydro(1)benzothieno(3,2‐g)(1,4)oxazonine‐5‐carbonitrile.

A. White, L. M. Engelhardt, C. Greenwood, 1989 .

Protein fluorescence of nicotinamide nucleotide-dependent dehydrogenases.

J. Holbrook, M. Gore, R. W. Evans, 1972, The Biochemical journal.

Photolytic studies on the carbon monoxide complex of sulphaemoglobin.

T. Brittain, C. Greenwood, 1982, The Biochemical journal.

The reaction of Pseudomonas aeruginosa cytochrome c oxidase with carbon monoxide.

M. Wilson, S. R. Parr, C. Greenwood, 1975, The Biochemical journal.

Investigations into the effect of acid on the spectral and kinetic properties of purple membrane from Halobacterium halobium.

M. Edgerton, T. Moore, C. Greenwood, 1980, Biochemical Journal.

Effects of zinc and other metal ions on the stability and activity of Escherichia coli alkaline phosphatase.

C. Trotman, C. Greenwood, 1971, The Biochemical journal.

Bis-methionine axial ligation of haem in bacterioferritin from Pseudomonas aeruginosa

G. Moore, A. Thomson, M. Cheesman, 1990, Nature.

Evidence for Mössbauer spectroscopy for different forms of iron core in Pseudomonas aeruginosa bacterial ferritin.

N. Reid, G. Moore, D. Dickson, 1990, Biochemical Journal.

NMR study of the structural characteristics of variants of yeast iso-1-cytochrome c in which unvaried aromatic residues have been substituted.

G. Moore, A. Mauk, M. Smith, 1991, European journal of biochemistry.

A two-state analysis of co-operative oxygen binding in the three human embryonic haemoglobins.

R. Weber, N. Watmough, O. Hofmann, 1997, The Biochemical journal.

Studies of cyanide binding to myeloperoxidase by electron paramagnetic resonance and magnetic circular dichroism spectroscopies

A. Segal, A. Thomson, D. Barber, 1982 .

Studies on heme d1 extracted from Pseudomonas aeruginosa nitrite reductase.

T. A. Walsh, A. Thomson, D. Barber, 1981, Journal of inorganic biochemistry.

LIGHT CURVES AND PERIOD CHANGES OF TYPE II CEPHEIDS IN THE GLOBULAR CLUSTERS M3 AND M5

M. Ireland, K. Kinemuchi, Wayne Osborn, 2010, 1003.5924.

Crystal structure of the di-haem cytochrome c peroxidase from Pseudomonas aeruginosa.

V. Fülöp, J. Hajdu, C. Ridout, 1995, Structure.

Kinetic studies on the reaction between cytochrome c oxidase and ferrocytochrome c.

M. Brunori, M. Wilson, E. Antonini, 1975, The Biochemical journal.

A characterization of ferric sulphaemoglobin

D. Barber, T. Brittain, C. Greenwood, 1982 .

A temperature-jump study of the reaction between azurin and cytochrome c-551 from Pseudomonas aeruginosa.

M. Brunori, T. Wilson, C. Greenwood, 1974, The Biochemical journal.

Spectroscopic studies of partially reduced forms of Wolinella succinogenes nitrite reductase

A. Thomson, R. Blackmore, P. Gadsby, 1990, FEBS letters.

Oxygen "pulsed" cytochrome c oxidase: functional properties and catalytic relevance.

M. Brunori, A. Colosimo, M. Wilson, 1977, Proceedings of the National Academy of Sciences of the United States of America.

The Dinuclear Center of Cytochrome bo3 from Escherichia coli

A. Thomson, M. Cheesman, R. Little, 1998, Journal of bioenergetics and biomembranes.

Electron-transfer reactions between redox proteins from a bacterium (Pseudomonas fluorescens) and mammalian-heart muscle.

E. Antonini, A. Agrò, L. Avigliano, 1971, European journal of biochemistry.

The rate of electron transfer between fungal laccase and reduced azurin or cytochrome c.

M. Brunori, E. Antonini, A. Agrò, 1971, Archives of biochemistry and biophysics.

The reaction of reduced cytochrome C oxidase with oxygen.

C. Greenwood, Q. H. Gibson, 1967, The Journal of biological chemistry.

Near-infrared magnetic and natural circular dichroism of cytochrome c oxidase.

A. Thomson, C. Greenwood, P. E. Gooding, 1980, The Biochemical journal.

Some Spectroscopic Views of the CuA, Site in Cytochrome c Oxidase Preparations a

C. P. Barrett, G. George, A. Thomson, 1988, Annals of the New York Academy of Sciences.

Electron paramagnetic resonance and magnetic circular dichroism studies of a hexa‐heme nitrite reductase from Wolinella succinogenes

A. Thomson, R. Blackmore, T. Brittain, 1987, FEBS letters.

Determination of the heme spin states in cytochrome c oxidase using magnetic circular dichroism

A. Thomson, T. Brittain, C. Greenwood, 1976, FEBS letters.

A study of the oxidized form of Pseudomonas aeruginosa cytochrome c-551 peroxidase with the use of magnetic circular dichroism.

A. Thomson, P. Gadsby, J. Peterson, 1984, The Biochemical journal.

ON THE MOLECULAR MECHANISM OF BIOLUMINESCENCE. I. THE ROLE OF LONG-CHAIN ALDEHYDE.

J. W. Hastings, Q. Gibson, C. Greenwood, 1964, Proceedings of the National Academy of Sciences of the United States of America.

The reaction of Escherichia coli cytochrome bo with H202: Evidence for the formation of an oxyferryl species by two distinct routes

R. Little, N. Watmough, T. Brittain, 1996, FEBS letters.

The formation of ferric haem during low-temperature photolysis of horseradish peroxidase Compound I.

M. Berry, A. Thomson, P. Gadsby, 1987, The Biochemical journal.

Complex formation between the copper protein, azurin and the cytochrome c peroxidase of Pseudomonas aeruginosa.

T. Brittain, C. Greenwood, 1992, Journal of inorganic biochemistry.

Cytochrome bo(3) from Escherichia coli: the binding and turnover of nitric oxide.

M. Arese, P. Sarti, E. Forte, 2002, Biochemical and biophysical research communications.

ON THE MOLECULAR MECHANISM OF BIOLUMINESCENCE, II. LIGHT-INDUCED LUMINESCENCE.

J. W. Hastings, Q. Gibson, C. Greenwood, 1965, Proceedings of the National Academy of Sciences of the United States of America.

Cytochromes c and Cytochrome c Containing Enzymes

C. Greenwood, 1985 .

Kinetic studies on (N-formyltryptophyl)cytochrome c.

T. Brittain, C. Greenwood, 1975, The Biochemical journal.

The preparation and some properties of mammalian cytochrome c modified with 2-hydroxy-5-nitrobenzyl bromide.

T. Brittain, C. Greenwood, 1975, The Biochemical journal.

A comparative study of some kinetic and spectral properties of guanidinated and native cytochrome c.

T. Brittain, C. Greenwood, 1975, The Biochemical journal.

Chromous ion reduction of mammalian cytochrome oxidase and some of its derivatives.

M. Brunori, M. Wilson, T. Brittain, 1977, The Biochemical journal.

Electron-paramagnetic-resonance and magnetic-circular-dichroism studies on the formate dehydrogenase-nitrate reductase particle from Pseudomonas aeruginosa.

A. Thomson, P. Gadsby, A. Coddington, 1987, The Biochemical journal.

KINETIC EVIDENCE FOR A SHORT LIVED INTERMEDIATE IN THE OXIDATION OF CYTOCHROME C OXIDASE BY MOLECULAR OXYGEN.

C. Greenwood, Q. H. Gibson, 1965, The Journal of biological chemistry.

The oxidation of Pseudomonas cytochrome c-551 oxidase by potassium ferricyanide.

D. Barber, S. R. Parr, C. Greenwood, 1978, The Biochemical journal.

pH-dependent forms of the ferryl haem in myoglobin peroxide analysed by variable-temperature magnetic circular dichroism.

A. Thomson, P. Gadsby, N. Foote, 1989, The Biochemical journal.

Salt reversal of the acid‐induced changes in purple membrane from halobacterium halobium

M. Edgerton, C. Greenwood, T. Moore, 1978, FEBS letters.

The reactions of Pseudomonas cytochrome c-551 oxidase with potassium cyanide.

D. Barber, S. R. Parr, C. Greenwood, 1978, The Biochemical journal.

The characterization and magnetic properties of the azide and imidazole derivatives of Pseudomonas nitrite reductase.

T. A. Walsh, A. Thomson, D. Barber, 1981, Journal of inorganic biochemistry.

The reaction of Pseudomonas aeruginosa cytochrome c oxidase with sodium metabisulphite (Short Communication)

Michael T. Wilson, S. R. Parr, C. Greenwood, 1974 .

Photolytic studies on cytochrome c peroxidase from Pseudomonas aeruginosa

A. Thomson, J. Peterson, N. Foote, 1985 .

The reduction of Pseudomonas cytochrome c551 oxidase by chromous ions.

D. Barber, S. R. Parr, C. Greenwood, 1977, The Biochemical journal.

Characterization of the partially reduced cyanide-inhibited derivative of cytochrome c oxidase by optical, electron-paramagnetic-resonance and magnetic-circular-dichroism spectroscopy.

A. Thomson, C. Greenwood, P. E. Gooding, 1981, The Biochemical journal.

Magnetic-circular-dichroism studies of haem a and its derivatives.

A. Thomson, T. Brittain, C. Greenwood, 1978, The Biochemical journal.